ID   ST1A1_RAT               Reviewed;         291 AA.
AC   P17988; Q548D2;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Sulfotransferase 1A1;
DE            Short=ST1A1;
DE            EC=2.8.2.1 {ECO:0000269|PubMed:1513323, ECO:0000269|PubMed:7889867, ECO:0000269|PubMed:8447833};
DE   AltName: Full=Aryl sulfotransferase;
DE   AltName: Full=Aryl sulfotransferase IV;
DE            Short=ASTIV;
DE   AltName: Full=Minoxidil sulfotransferase {ECO:0000303|PubMed:1513323};
DE            Short=Mx-ST {ECO:0000303|PubMed:1513323};
DE   AltName: Full=PST-1 {ECO:0000303|PubMed:2374726};
DE   AltName: Full=Phenol sulfotransferase;
DE   AltName: Full=Sulfokinase;
DE   AltName: Full=Tyrosine-ester sulfotransferase;
GN   Name=Sult1a1; Synonyms=St1a1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=2374726; DOI=10.1093/nar/18.13.4001;
RA   Ozawa S., Nagata K., Gong D., Yamazoe Y., Kato R.;
RT   "Nucleotide sequence of a full-length cDNA (PST-1) for aryl
RT   sulfotransferase from rat liver.";
RL   Nucleic Acids Res. 18:4001-4001(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=1513323;
RA   Hirshey S.J., Dooley T.P., Reardon I.M., Heinrikson R.L., Falany C.N.;
RT   "Sequence analysis, in vitro translation and expression of the cDNA for rat
RT   liver minoxidil sulfotransferase.";
RL   Mol. Pharmacol. 42:257-264(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8299966; DOI=10.1016/0378-1119(93)90028-2;
RA   Khan A.S., Taylor B.R., Chung K., Etheredge J., Gonzales R., Ringer D.P.;
RT   "Genomic structure of rat liver aryl sulfotransferase IV-encoding gene.";
RL   Gene 137:321-326(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Mao C., Sanchez R.I., Clairmont K., Coughtrie M.W.H., Kauffman F.C.;
RT   "Cloning, bacterial expression and characterization of rat brain phenol
RT   sulfotransferase SULT1A1: an enzyme involved in neurosteroid and dopamine
RT   sulfonation.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-291.
RX   PubMed=1511441;
RA   Yerokun T., Etheredge J.L., Norton T.R., Carter H.A., Chung K.H.,
RA   Birckbichler P.J., Ringer D.P.;
RT   "Characterization of a complementary DNA for rat liver aryl
RT   sulfotransferase IV and use in evaluating the hepatic gene transcript
RT   levels of rats at various stages of 2-acetylaminofluorene-induced
RT   hepatocarcinogenesis.";
RL   Cancer Res. 52:4779-4786(1992).
RN   [6]
RP   PROTEIN SEQUENCE OF 63-68, AND CHARACTERIZATION.
RX   PubMed=7982943; DOI=10.1016/s0021-9258(18)43814-8;
RA   Zheng Y., Bergold A., Duffel M.W.;
RT   "Affinity labeling of aryl sulfotransferase IV. Identification of a peptide
RT   sequence at the binding site for 3'-phosphoadenosine-5'-phosphosulfate.";
RL   J. Biol. Chem. 269:30313-30319(1994).
RN   [7]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RC   TISSUE=Liver;
RX   PubMed=8447833; DOI=10.1006/bbrc.1993.1216;
RA   Cruickshank D., Sansom L.N., Veronese M.E., Mojarrabi B., McManus M.E.,
RA   Zhu X.;
RT   "cDNA expression studies of rat liver aryl sulphotransferase.";
RL   Biochem. Biophys. Res. Commun. 191:295-301(1993).
RN   [8]
RP   CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=7889867; DOI=10.1289/ehp.94102s699;
RA   Yamazoe Y., Ozawa S., Nagata K., Gong D.-W., Kato R.;
RT   "Characterization and expression of hepatic sulfotransferase involved in
RT   the metabolism of N-substituted aryl compounds.";
RL   Environ. Health Perspect. 102:99-103(1994).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=8033271; DOI=10.1016/0009-2797(94)90054-x;
RA   Runge-Morris M.A.;
RT   "Sulfotransferase gene expression in rat hepatic and extrahepatic
RT   tissues.";
RL   Chem. Biol. Interact. 92:67-76(1994).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide
CC       variety of acceptor molecules bearing a hydroxyl or an amine groupe.
CC       Sulfonation increases the water solubility of most compounds, and
CC       therefore their renal excretion, but it can also result in
CC       bioactivation to form active metabolites. Displays broad substrate
CC       specificity for small phenolic compounds (PubMed:8447833,
CC       PubMed:7889867, PubMed:1513323). Plays an important roles in the
CC       sulfonation of endogenous molecules such as steroid hormones and 3,3'-
CC       diiodothyronin (By similarity). Mediates the sulfate conjugation of a
CC       variety of xenobiotics, including the drugs acetaminophen and minoxidil
CC       (PubMed:1513323). Mediates also the metabolic activation of
CC       carcinogenic N-hydroxyarylamines leading to highly reactive
CC       intermediates capable of forming DNA adducts, potentially resulting in
CC       mutagenesis (By similarity). May play a role in gut microbiota-host
CC       metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary
CC       tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS
CC       crosses the blood-brain barrier and may negatively regulate
CC       oligodendrocyte maturation and myelination, affecting the functional
CC       connectivity of different brain regions associated with the limbic
CC       system. {ECO:0000250|UniProtKB:P50225, ECO:0000269|PubMed:1513323,
CC       ECO:0000269|PubMed:7889867, ECO:0000269|PubMed:8447833}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC         bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC         Evidence={ECO:0000269|PubMed:1513323, ECO:0000269|PubMed:7889867,
CC         ECO:0000269|PubMed:8447833};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta-
CC         estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + 4-ethylphenol = 4-ethylphenyl
CC         sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:70607,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:49584, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:133681;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70608;
CC         Evidence={ECO:0000250|UniProtKB:P50225};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P50225}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1513323}.
CC   -!- TISSUE SPECIFICITY: Liver, kidney, heart and colon.
CC       {ECO:0000269|PubMed:8033271}.
CC   -!- INDUCTION: Induced by androgens and suppressed by estrogens. The
CC       expression is under the influence of pituitary growth hormone and
CC       thyroid hormone.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR   EMBL; X52883; CAA37065.1; -; mRNA.
DR   EMBL; L19998; AAA41644.1; -; mRNA.
DR   EMBL; L16241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF394783; AAK77559.1; -; mRNA.
DR   EMBL; X68640; CAA48604.1; -; mRNA.
DR   PIR; S10329; S10329.
DR   RefSeq; NP_114022.1; NM_031834.1.
DR   AlphaFoldDB; P17988; -.
DR   SMR; P17988; -.
DR   STRING; 10116.ENSRNOP00000026186; -.
DR   ChEMBL; CHEMBL4886; -.
DR   iPTMnet; P17988; -.
DR   PhosphoSitePlus; P17988; -.
DR   PaxDb; 10116-ENSRNOP00000026186; -.
DR   Ensembl; ENSRNOT00000026186.5; ENSRNOP00000026186.1; ENSRNOG00000019342.5.
DR   Ensembl; ENSRNOT00055045066; ENSRNOP00055036964; ENSRNOG00055026108.
DR   Ensembl; ENSRNOT00060052281; ENSRNOP00060043503; ENSRNOG00060030085.
DR   Ensembl; ENSRNOT00065027878; ENSRNOP00065021998; ENSRNOG00065016720.
DR   GeneID; 83783; -.
DR   KEGG; rno:83783; -.
DR   UCSC; RGD:3767; rat.
DR   AGR; RGD:3767; -.
DR   CTD; 6817; -.
DR   RGD; 3767; Sult1a1.
DR   eggNOG; KOG1584; Eukaryota.
DR   GeneTree; ENSGT00940000162765; -.
DR   HOGENOM; CLU_027239_1_2_1; -.
DR   InParanoid; P17988; -.
DR   OMA; CISKQTH; -.
DR   OrthoDB; 3083090at2759; -.
DR   PhylomeDB; P17988; -.
DR   TreeFam; TF321745; -.
DR   BRENDA; 2.8.2.1; 5301.
DR   Reactome; R-RNO-156584; Cytosolic sulfonation of small molecules.
DR   Reactome; R-RNO-9753281; Paracetamol ADME.
DR   PRO; PR:P17988; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019342; Expressed in liver and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; IDA:RGD.
DR   GO; GO:0004062; F:aryl sulfotransferase activity; IDA:RGD.
DR   GO; GO:0047894; F:flavonol 3-sulfotransferase activity; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0050294; F:steroid sulfotransferase activity; ISO:RGD.
DR   GO; GO:0008146; F:sulfotransferase activity; IDA:RGD.
DR   GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; ISO:RGD.
DR   GO; GO:0018960; P:4-nitrophenol metabolic process; IDA:RGD.
DR   GO; GO:0006584; P:catecholamine metabolic process; IDA:RGD.
DR   GO; GO:0008210; P:estrogen metabolic process; IMP:RGD.
DR   GO; GO:0006068; P:ethanol catabolic process; ISO:RGD.
DR   GO; GO:0009812; P:flavonoid metabolic process; ISO:RGD.
DR   GO; GO:0008217; P:regulation of blood pressure; IEP:RGD.
DR   GO; GO:0014823; P:response to activity; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IMP:RGD.
DR   GO; GO:0017085; P:response to insecticide; IEP:RGD.
DR   GO; GO:0051923; P:sulfation; IDA:RGD.
DR   GO; GO:0042403; P:thyroid hormone metabolic process; ISS:UniProtKB.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IDA:RGD.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR11783:SF324; SULFOTRANSFERASE 1A3-RELATED; 1.
DR   PANTHER; PTHR11783; SULFOTRANSFERASE SULT; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; P17988; RN.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Lipid metabolism; Phosphoprotein;
KW   Reference proteome; Steroid metabolism; Transferase.
FT   CHAIN           1..291
FT                   /note="Sulfotransferase 1A1"
FT                   /id="PRO_0000085131"
FT   ACT_SITE        104
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         44..49
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         102..104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         126
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         134
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         189
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         223..228
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   BINDING         251..255
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250|UniProtKB:P50225"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   291 AA;  33906 MW;  9EC66C72923DB872 CRC64;
     MEFSRPPLVH VKGIPLIKYF AETIGPLQNF TAWPDDLLIS TYPKSGTTWM SEILDMIYQG
     GKLEKCGRAP IYARVPFLEF KCPGVPSGLE TLEETPAPRL LKTHLPLSLL PQSLLDQKVK
     VIYIARNAKD VVVSYYNFYN MAKLHPDPGT WDSFLENFMD GEVSYGSWYQ HVKEWWELRH
     THPVLYLFYE DIKENPKREI KKILEFLGRS LPEETVDSIV HHTSFKKMKE NCMTNYTTIP
     TEIMDHNVSP FMRKGTTGDW KNTFTVAQNE RFDAHYAKTM TDCDFKFRCE L
//